Linked Life Data

6111625

Source:http://linkedlifedata.com/resource/pubmed/id/6111625

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1981-6-25
pubmed:abstractText
An Mg2+-dependent low ATPase activity can be detected in erythrocyte "white membranes," in addition to that of the well known (Ca2+ + Mg2+)-ATPase. The thiol oxidizing agent diamide affects both activities. The oxidation of neighboring thiols seems to leave the mechanism of the (Ca2+ + Mg2+)-ATPase amplification system evoked by Ca2+ largely unaffected. The perturbation caused by diamide in the membranes seems to affect primarily a step of the ATP hydrolysis mechanism that is common to both ATPase activities. The effectiveness of diamide seems to be the same when either Ca2+ and Mg2+, or Mg2+ alone are present during the reagent action. Reduction of disulfide bonds by DTE after diamide treatment restores the (Ca2+ + Mg2+)-ATPase activity but is unable to take the Mg2+-ATPase activity back to the original level. The hypothesis is discussed that the redox state of one (or more than one) couple of --SH close to each other and possibly connected to the active site, may be an important factor in optimizing the efficiency of Ca action on the (Ca2+ + Mg2+)-ATPase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0091-7419
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-11
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Divalent cation dependent ATPase activities of red blood cell membranes: influence of the oxidation of membrane thiol groups close to each other.
pubmed:publicationType
Journal Article